title: Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver.
abstract: The cytoplasmic B-type histone acetyltransferase was purified to apparent homogeneity from maize embryos. We established a novel protocol for easy large-scale preparation of acetylated core histone species, using preparative acetic acid-urea-Triton PAGE. The pure maize histone acetyltransferase B was highly specific for histone H4 under various assay conditions, modifying H4 up to the di-acetylated isoform. Only non-acetylated H4 isoform was accepted as substrate, whereas mono-acetylated H4 could not be further acetylated. The enzyme selectively acetylated lysines 12 and 5 in a sequential manner. The same results were obtained with a partially purified cytoplasmic histone acetyltransferase of rat liver. Protein sequencing results were supported by immunological characterization of acetylated H4 subspecies with site-specific H4-acetyllysine antibodies.
authors.affiliation: Department of Microbiology, University of Innsbruck Medical School, Austria.
authors.forename: D
authors.initials: D
authors.lastname: Kölle
authors.forename: B
authors.initials: B
authors.lastname: Sarg
authors.forename: H
authors.initials: H
authors.lastname: Lindner
authors.forename: P
authors.initials: P
authors.lastname: Loidl
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D003593:Cytoplasm; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D003313:Zea mays / Q000201:enzymology*
chemical_list: D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases